ID Q6A7Z5_CUTAK Unreviewed; 429 AA.
AC Q6A7Z5;
DT 13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2004, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE SubName: Full=Thymidine phosphorylase {ECO:0000313|EMBL:AAT83120.1};
DE EC=2.4.2.4 {ECO:0000313|EMBL:AAT83120.1};
GN OrderedLocusNames=PPA1367 {ECO:0000313|EMBL:AAT83120.1};
OS Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS acnes).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Cutibacterium.
OX NCBI_TaxID=267747 {ECO:0000313|EMBL:AAT83120.1, ECO:0000313|Proteomes:UP000000603};
RN [1] {ECO:0000313|EMBL:AAT83120.1, ECO:0000313|Proteomes:UP000000603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16379 / KPA171202 {ECO:0000313|Proteomes:UP000000603};
RX PubMed=15286373; DOI=10.1126/science.1100330;
RA Bruggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA Strittmatter A., Hujer S., Durre P., Gottschalk G.;
RT "The complete genome sequence of Propionibacterium acnes, a commensal of
RT human skin.";
RL Science 305:671-673(2004).
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC phosphorylase family. {ECO:0000256|ARBA:ARBA00006915}.
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DR EMBL; AE017283; AAT83120.1; -; Genomic_DNA.
DR RefSeq; WP_002516498.1; NZ_CP025935.1.
DR AlphaFoldDB; Q6A7Z5; -.
DR EnsemblBacteria; AAT83120; AAT83120; PPA1367.
DR GeneID; 66620798; -.
DR KEGG; pac:PPA1367; -.
DR eggNOG; COG0213; Bacteria.
DR HOGENOM; CLU_025040_0_1_11; -.
DR Proteomes; UP000000603; Chromosome.
DR GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; IEA:InterPro.
DR GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:InterPro.
DR GO; GO:0009032; F:thymidine phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
DR GO; GO:0006213; P:pyrimidine nucleoside metabolic process; IEA:InterPro.
DR Gene3D; 3.40.1030.10; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR Gene3D; 3.90.1170.30; Pyrimidine nucleoside phosphorylase-like, C-terminal domain; 1.
DR InterPro; IPR000312; Glycosyl_Trfase_fam3.
DR InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom.
DR InterPro; IPR036320; Glycosyl_Trfase_fam3_N_dom_sf.
DR InterPro; IPR035902; Nuc_phospho_transferase.
DR InterPro; IPR036566; PYNP-like_C_sf.
DR InterPro; IPR013102; PYNP_C.
DR InterPro; IPR018090; Pyrmidine_PPas_bac/euk.
DR InterPro; IPR017872; Pyrmidine_PPase_CS.
DR InterPro; IPR000053; Thymidine/pyrmidine_PPase.
DR NCBIfam; TIGR02644; Y_phosphoryl; 1.
DR PANTHER; PTHR10515; THYMIDINE PHOSPHORYLASE; 1.
DR PANTHER; PTHR10515:SF0; THYMIDINE PHOSPHORYLASE; 1.
DR Pfam; PF02885; Glycos_trans_3N; 1.
DR Pfam; PF00591; Glycos_transf_3; 1.
DR Pfam; PF07831; PYNP_C; 1.
DR PIRSF; PIRSF000478; TP_PyNP; 1.
DR SMART; SM00941; PYNP_C; 1.
DR SUPFAM; SSF52418; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR SUPFAM; SSF47648; Nucleoside phosphorylase/phosphoribosyltransferase N-terminal domain; 1.
DR SUPFAM; SSF54680; Pyrimidine nucleoside phosphorylase C-terminal domain; 1.
DR PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:AAT83120.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AAT83120.1}.
FT DOMAIN 338..412
FT /note="Pyrimidine nucleoside phosphorylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00941"
SQ SEQUENCE 429 AA; 44692 MW; 50D1748FF92BADA9 CRC64;
MTSTYSVVDL IRAKREGQTL NSDQIAWLIR AYTDDIVADE QMSAMAMAVY FQGLDDAELS
AWTTAMIKSG ERMSFAGLSR PTVDKHSTGG VGDKITLPLA PLVAACGAAV PQLSGRGLGH
TGGTLDKMEA IPGWRADLSH DEMVAQLEKV GAVICAAGPG LAPADKKLYA LRDVTGTVES
IPLIASSIMS KKIAEGTDSL VLDVKTGSGA FMKTDKDARE LASRLVELGE AAGVRTTALL
THMDVPLGYA CGNGIEVAES LEVLAGGGPA DVVELTVALA RHMVKVAGLD GIDPADVLAS
GQAMDVWRNM VRAQGGDPDA PLPMAHHTQD IVATEAGVIT GIDAMSVGLA AWRLGAGRAR
KEDPVQAAAG IMLRVRPGDR VVTGQPLATL LTDTPDSIAR AEDAMTNAFT VGQTFQPQDI
VIDTVVAQS
//
